ID   ASF1_ENCCU              Reviewed;         292 AA.
AC   Q8SRM1;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Histone chaperone ASF1;
DE   AltName: Full=Anti-silencing function protein 1;
GN   Name=ASF1; OrderedLocusNames=ECU07_0130;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
CC   -!- FUNCTION: Histone chaperone that facilitates histone deposition and
CC       histone exchange and removal during nucleosome assembly and
CC       disassembly. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with histone H3 and histone H4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
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DR   EMBL; AL590447; CAD25545.1; -; Genomic_DNA.
DR   RefSeq; NP_585941.1; NM_001041563.1.
DR   AlphaFoldDB; Q8SRM1; -.
DR   SMR; Q8SRM1; -.
DR   STRING; 284813.Q8SRM1; -.
DR   GeneID; 859369; -.
DR   KEGG; ecu:ECU07_0130; -.
DR   VEuPathDB; MicrosporidiaDB:ECU07_0130; -.
DR   HOGENOM; CLU_083062_0_0_1; -.
DR   InParanoid; Q8SRM1; -.
DR   OrthoDB; 1350132at2759; -.
DR   Proteomes; UP000000819; Chromosome VII.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0016573; P:histone acetylation; IEA:InterPro.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0006337; P:nucleosome disassembly; IEA:InterPro.
DR   Gene3D; 2.60.40.1490; -; 1.
DR   InterPro; IPR006818; ASF1-like.
DR   InterPro; IPR036747; ASF1-like_sf.
DR   InterPro; IPR017282; Hist_deposition_Asf1.
DR   PANTHER; PTHR12040; PTHR12040; 1.
DR   Pfam; PF04729; ASF1_hist_chap; 1.
DR   PIRSF; PIRSF037759; Histone_Asf1; 1.
DR   SUPFAM; SSF101546; SSF101546; 1.
PE   3: Inferred from homology;
KW   Chaperone; Chromatin regulator; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..292
FT                   /note="Histone chaperone ASF1"
FT                   /id="PRO_0000284036"
FT   REGION          123..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..173
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..292
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   292 AA;  32962 MW;  1ECAD20CCA3421F0 CRC64;
     MGHLKLKSIE VDSTVKKLGD PLKFNLRFVC FEEIKCGVEF VVLYNMDVHS DENDQVLAEI
     EVAPIPKGKI EFSIDADAPD VNKIPLDEMF GLTSILIVGR YKGQQFIRIG YIVDVGYPGI
     PSTKLMKSDV EEPSEEIGDK EEEDEEDVEE ELGSEEGSEE SSCIVEDKDE DNEEAEPRTF
     MEAVEDVGNE GKERLFESEG REEEEDEKVG SDSYSEVNRE LNKSVGEEAE GSDGGEDVVD
     YCGFRIDKKQ IEMKLMDPPV INLFEIEWEE ESPSEEVPRN NNESPAKKQK VE